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CAZyme Information: MGYG000003064_01880

You are here: Home > Sequence: MGYG000003064_01880

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Bacteroides graminisolvens
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides graminisolvens
CAZyme ID MGYG000003064_01880
CAZy Family GH67
CAZyme Description Extracellular xylan exo-alpha-(1->2)-glucuronosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
686 MGYG000003064_6|CGC7 77929.67 7.0072
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003064 3410784 MAG United States North America
Gene Location Start: 197272;  End: 199332  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.139 3.2.1.131 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH67 64 658 4.6e-285 0.8863976083707026

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3661 AguA2 0.0 17 659 2 677
Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488 Glyco_hydro_67M 0.0 112 430 1 324
Glycosyl hydrolase family 67 middle domain. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuronidase.
pfam07477 Glyco_hydro_67C 4.13e-124 432 662 1 223
Glycosyl hydrolase family 67 C-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C terminal region of alpha-glucuronidase which is mainly alpha-helical. It wraps around the catalytic domain (pfam07488), making additional interactions both with the N-terminal domain (pfam03648) of its parent monomer and also forming the majority of the dimer-surface with the equivalent C-terminal domain of the other monomer of the dimer.
pfam03648 Glyco_hydro_67N 7.12e-09 25 109 1 120
Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT24930.1 0.0 18 685 19 708
QUR44061.1 0.0 18 685 19 708
CBK69516.1 0.0 18 685 19 708
QIU96895.1 0.0 16 685 16 716
QRN00781.1 0.0 18 685 19 708

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1GQI_A 1.73e-252 44 672 35 686
Structureof Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQI_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQJ_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQJ_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQK_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQK_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQL_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus],1GQL_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus]
1H41_A 1.40e-251 44 672 35 686
Pseudomonascellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid [Cellvibrio japonicus],1H41_B Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid [Cellvibrio japonicus]
1MQP_A 1.82e-192 37 653 25 667
TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1K9D_A 2.57e-192 37 653 25 667
The1.7 A crystal structure of alpha-D-glucuronidase, a family-67 glycoside hydrolase from Bacillus stearothermophilus T-1 [Geobacillus stearothermophilus],1L8N_A The 1.5A crystal structure of alpha-D-glucuronidase from Bacillus stearothermophilus T-1, complexed with 4-O-methyl-glucuronic acid and xylotriose [Geobacillus stearothermophilus],1MQQ_A THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM BACILLUS STEAROTHERMOPHILUS T-1 COMPLEXED WITH GLUCURONIC ACID [Geobacillus stearothermophilus]
1MQR_A 5.15e-192 37 653 25 667
ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B3PC73 5.38e-252 4 672 8 710
Extracellular xylan exo-alpha-(1->2)-glucuronosidase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=gla67A PE=1 SV=1
Q09LY5 9.95e-192 37 653 25 667
Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105 2.61e-182 71 666 78 673
Xylan alpha-(1->2)-glucuronosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=aguA PE=1 SV=2
Q5AQZ4 3.31e-145 75 674 109 720
Alpha-glucuronidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aguA PE=1 SV=1
A1CC12 8.39e-144 75 653 109 684
Probable alpha-glucuronidase A OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=aguA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000301 0.999008 0.000189 0.000165 0.000159 0.000150

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003064_01880.